Three-dimensional conformation of the epitopes of human superoxide dismutase-2 recognized by antibody against HIV-1p17.
- Authors:
- Published online on: January 1, 1998 https://doi.org/10.3892/ijmm.1.1.63
- Pages: 63-69
Metrics: Total
Views: 0 (Spandidos Publications: | PMC Statistics: )
Total PDF Downloads: 0 (Spandidos Publications: | PMC Statistics: )
Abstract
We have previously reported that antibodies against HIV-1p17 protein cross-react with human superoxide dismutase-2 (SOD-2). To identify and characterize the epitopes of human SOD-2 recognized by anti-HIV-1p17 antibody, we synthesized several peptide fragments of human SOD-2 and found that the antibody did not bind to the LQPALK hexapeptide which is contained in both HIV-1p17 and human SOD-2. Instead, this antibody bound to four peptides which contain amino acid sequences similar, but not identical, to the known epitopes of HIV-1p17. These peptides have two features in three-dimensional (3-D) conformation: two protruded carbohydrate side chains on the peptide chain or a concave structure in the molecule. It is suggested that the antibody does not strictly recognize the amino acid sequence itself, but may recognize these 3-D conformations.